1pw4
From Proteopedia
(New page: 200px<br /><applet load="1pw4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pw4, resolution 3.3Å" /> '''Crystal Structure of ...) |
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| - | [[Image:1pw4.jpg|left|200px]]<br /><applet load="1pw4" size=" | + | [[Image:1pw4.jpg|left|200px]]<br /><applet load="1pw4" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1pw4, resolution 3.3Å" /> | caption="1pw4, resolution 3.3Å" /> | ||
'''Crystal Structure of the Glycerol-3-Phosphate Transporter from E.Coli'''<br /> | '''Crystal Structure of the Glycerol-3-Phosphate Transporter from E.Coli'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The major facilitator superfamily represents the largest group of | + | The major facilitator superfamily represents the largest group of secondary membrane transporters in the cell. Here we report the 3.3 angstrom resolution structure of a member of this superfamily, GlpT, which transports glycerol-3-phosphate into the cytoplasm and inorganic phosphate into the periplasm. The amino- and carboxyl-terminal halves of the protein exhibit a pseudo two-fold symmetry. Closed off to the periplasm, a centrally located substrate-translocation pore contains two arginines at its closed end, which comprise the substrate-binding site. Upon substrate binding, the protein adopts a more compact conformation. We propose that GlpT operates by a single-binding site, alternating-access mechanism through a rocker-switch type of movement. |
==About this Structure== | ==About this Structure== | ||
| - | 1PW4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1PW4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PW4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Auer, M.]] | [[Category: Auer, M.]] | ||
[[Category: Huang, Y.]] | [[Category: Huang, Y.]] | ||
| - | [[Category: Lemieux, M | + | [[Category: Lemieux, M J.]] |
[[Category: Song, J.]] | [[Category: Song, J.]] | ||
| - | [[Category: Wang, D | + | [[Category: Wang, D N.]] |
[[Category: glycerol-3-phosphate]] | [[Category: glycerol-3-phosphate]] | ||
[[Category: inner membrane]] | [[Category: inner membrane]] | ||
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[[Category: transporter]] | [[Category: transporter]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:33:07 2008'' |
Revision as of 12:33, 21 February 2008
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Crystal Structure of the Glycerol-3-Phosphate Transporter from E.Coli
Overview
The major facilitator superfamily represents the largest group of secondary membrane transporters in the cell. Here we report the 3.3 angstrom resolution structure of a member of this superfamily, GlpT, which transports glycerol-3-phosphate into the cytoplasm and inorganic phosphate into the periplasm. The amino- and carboxyl-terminal halves of the protein exhibit a pseudo two-fold symmetry. Closed off to the periplasm, a centrally located substrate-translocation pore contains two arginines at its closed end, which comprise the substrate-binding site. Upon substrate binding, the protein adopts a more compact conformation. We propose that GlpT operates by a single-binding site, alternating-access mechanism through a rocker-switch type of movement.
About this Structure
1PW4 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure and mechanism of the glycerol-3-phosphate transporter from Escherichia coli., Huang Y, Lemieux MJ, Song J, Auer M, Wang DN, Science. 2003 Aug 1;301(5633):616-20. PMID:12893936
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